LH1 ARG670END
SiMPLOD ID   This is the unique identifier for this mutation in the SiMPLOD database. Please use this identifier when linking information described in SiMPLOD about this mutation.	SiMPLOD1-51
Isoenzyme   Follow the links to gather information about the LH1 isoenzyme	Lysyl Hydroxylase 1 (human) - UniProt - Full Info
Nucleotide mutation   Follow the links to explore annotated information about the significance of the PLOD1 c.2008C>T mutation	PLOD1 NM_000302.2:c.2008C>T - NCBI RefSeq NCBI SNP: rs121913554 NCBI ClinVar: 14373
Mutation type   Current information about the clinical implications of the mutation	Pathogenic
LOVD   Link to Leiden Open Variation Database (LOVD)	c.2032C>T
Disease Phenotype   Annotated information about disease phenotypes associated to this mutation	Kyphoscoliotic Ehlers-Danlos Syndrome (Type VIa) Link1 Link2
Clinical Databases   Link to clinical databases, including OMIM (Online Mendelian Inheritance in Man), Orphanet, ICD-10 (International Statistical Classification of Diseases and Related Health Problems, rev. 10), MeSH (Medical Subject Headings)	OMIM: 225400 Orphanet: ORPHA:1900 ICD-10: Q79.6 MeSH: C536198
Evidence at protein level   Based on available structural and biochemical information, a statement about the existence of an LH enzyme variant bearing the described mutation is provided	Warning: this variant incorporates a premature truncation of the aminoacid sequence at residue 670, and may result in misfolding and/or complete absence of the enzyme. This variant is EXTREMELY UNLIKELY to be compatible with a folded LH enzyme. The representation shown in the structure viewer is therefore for mere display purposes and does not refer to an actual predicted existing protein product.
References   Publications (and associated links) describing the mutation	Yeowell et al., 2000 - DOI - PubMed
Notes from publications   A curated excerpt with information about the mutation from the publications found above	Screening PLOD1 cDNA in fibroblast from Ehlers-Danlos syndrome type VI (EDS VI) patients Yeowell et al. identified four novel disease causing mutations. Among these, the point mutation c.2032C>T was predicted to produce the premature termination codon Arg670End in exon 18 causing an almost total deletion of the c-terminal catalytic domain.
Structural Observations   An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure
Related Entries   A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized	SiMPLOD2-1028: LH2a ASN680ASN (SNP)
Last Update   An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure	2021-06-23 08:38:51
The three-dimensional visualization is currently based on the homology model of full-length, dimeric human LH1 (generated using the crystal structure of full-length human LH3 as template). You may select a different PDB model file to visualize the mutation(s) using the drop-down menu below (page will refresh): LH1 homology modelLH3 with Fe2+ and 2-OG (PDB 6FXK)